P31comet, a member of the synaptonemal complex, participates in meiotic DSB formation in rice

P31comet, a member of the synaptonemal complex, participates in meiotic DSB formation in rice
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P31(彗星)是联会复合体的成员,参与水稻减数分裂 DSB 的形成。

DOI:
10.1073/pnas.1607334113
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发表时间:
2016-09-20
影响因子:
11.1
通讯作者:
Cheng, Zhukuan
Cheng, Zhukuan
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Ji, Jianhui;Tang, Ding;Cheng, Zhukuan

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人有丝分裂阻滞缺陷2(Mad2)结合蛋白p31(彗星)参与纺锤体检查点并协调有丝分裂中的细胞周期事件,尽管其在减数分裂中的功能在所有生物体中仍然未知。在这里,我们揭示p31(彗星)作为联会复合体(SC)蛋白在水稻(Oryza sativa L.)。在p31(彗星)中,同源配对和突触被消除,导致同源不分离和完全不育。组蛋白H2AX磷酸化(. H2AX)在p31(comet)中的装载失败,以及水稻减数分裂重组1(com1)p31(comet)和辐射敏感51 c(rad51 c)p31(comet)双突变体的染色体断裂被抑制,表明p31(comet)在双链断裂(DSB)形成中起重要作用。有趣的是,p31(彗星)和ZEP 1(SC的横丝蛋白)之间的动态共定位模式的免疫染色,以及p31(彗星)和中央区组件1(CRC 1)之间的相互作用,在酵母双杂交试验,表明可能参与的p31(彗星)在SC安装。总之,这些数据表明,p31(彗星)在DSB形成和SC安装中起着关键作用,主要是通过与CRC1的合作。
The human mitotic arrest-deficient 2 (Mad2) binding protein p31(comet) participates in the spindle checkpoint and coordinates cell cycle events in mitosis although its function in meiosis remains unknown in all organisms. Here, we reveal p31(comet) as a synaptonemal complex (SC) protein in rice (Oryza sativa L.). In p31(comet), homologous pairing and synapsis are eliminated, leading to the homologous nondisjunction and complete sterility. The failure in loading of histone H2AX phosphorylation (.H2AX) in p31(comet), together with the suppressed chromosome fragmentation in rice completion of meiotic recombination 1 (com1) p31(comet) and radiation sensitive 51c (rad51c) p31(comet) double mutants, indicates that p31(comet) plays an essential role in double-strand break (DSB) formation. Interestingly, the dynamic colocalization pattern between p31(comet) and ZEP1 (a transverse filament protein of SC) by immunostaining, as well as the interaction between p31(comet) and CENTRAL REGION COMPONENT 1 (CRC1) in yeast two-hybrid assays, suggests possible involvement of p31(comet) in SC installation. Together, these data indicate that p31(comet) plays a key role in DSB formation and SC installation, mainly through its cooperation with CRC1.